Bovine kidney low molecular weight acid phosphatase: FMN‐dependent kinetics

Granjeiro, José Mauro; Ferreira, Carmen Verı́ssima; Jucá, Marilena B.; Taga, Eulázio Mikio; Aoyama, Hiroshi

doi:10.1080/15216549700202291

Cited by 23 publications

(31 citation statements)

References 9 publications

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“…Some substrates that are present in the cellular metabolism, or natural substrates, were hydrolyzed at similar rates as that of the synthetic one. The efficient rate of hydrolysis of the natural substrates β-glycerol phosphate and FMN found in this study was also observed for acid phosphatases extracted from Chlamydomonas reinhardtii (Matagne et al, 1976) and from bovine kidney (Granjeiro et al, 1997). Similar enzymatic activities were reported for the cleavage of D-glucose 6-phosphate, D-fructose 6-phosphate and 5´AMP by the acid phosphatase extracted from de algae Enteromorpha linza (Yamamoto, 1972).…”

Section: Cleavage Of Substrates and Phosphatase Inhibitionsupporting

confidence: 69%

“…The activation energy obtained in our experiments (37.94 kJ mol ) is similar to those described by Lien & Knutsen (1973) for phosphatases extracted from the green algae C. reinhardtii (44.73 kJ mol -1 ) and for the acid phosphatases from other organisms, for example, bovine kidney (45.44 kJ mol -1 ) (Granjeiro et al, 1997). The activation energy value obtained for the acid phosphatase in this work is also closed to the values reported for other algae enzymes, such as hydrogenase (Schnackenberg et al, 1993) and urate oxidase (Alamillo et al, 1991) …”

Section: Kinetics Studiessupporting

confidence: 69%

“…The main objective was to compare the activity of the three extraction methods applied for the same extract, so the determination of protein for the specific activity calculation was unnecessary. Some authors expressed the enzyme activity by the absorbance or used this parameter to calculate the relative activity (%) in which the control is taken as 100% (Granjeiro et al, 1997;Demeke et al, 2001;Amani et al, 2005;Jonsson & Aoyama, 2007). In this study, we adopted similar assumptions for other experiments.…”

Section: Discussion Extractionmentioning

confidence: 99%

“…This element, as well as other metals, can intensify the production of reactive oxygen species (ROS) in soil (Gratão et al, 2005) and in aquatic organisms (Verlecar et al, 2008). ROS toxicity can be avoided by antioxidant enzymes like ascorbate peroxidase, superoxide dismutase and catalase, which are associated to Hg 2+ and Ni 2+ stress in algae (Okamoto et al, 2001;Huang et al, 2006) and in plants (Pompeu et al, 2008), respectively.…”

Section: Introductionmentioning

confidence: 99%

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Extraction, partial characterization and susceptibility to Hg2+ of acid phosphatase from the microalgae Pseudokirchneriella subcapitata

Jonsson¹,

Aoyama

2009

Sci. agric. (Piracicaba, Braz.)

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Pseudokirchneriella subcapitata is a unicellular green algae widely distributed in freshwater and soils. Due to its cosmopolitan characteristic, its use is recommended by national and international protocols in ecotoxicity studies. The alteration of phosphatase activities by agriculture pollutants like heavy metals has been extensively used as a biomarker in risk assessment and biomonitoring. In this study, we compared the extraction of acid phosphatase from P. subcapitata by different procedures and we studied the stability, substrates specificity, kinetics and the effect of Hg 2+ in the crude extract. The freezing and thawing technique associated with probe sonication was the most suitable method of extraction. The enzyme was stable when frozen at -20ºC for at least six months, showed an optimum pH of 5 and a Km value of 0.27 mM for p-nitrophenylphosphate (pNPP) as substrate. Some natural organic substrates were cleaved by a similar extent as the synthetic substrate pNPP. RESUMO: Pseudokirchneriella subcapitata é uma alga verde unicelular amplamente distribuída em corpos d´agua e solos. Devido a sua natureza cosmopolita, seu uso é recomendado por protocolos nacionais e internacionais na realização de estudos de ecotoxicidade. A alteração da atividade de fosfatases por agentes poluentes de origem agrícola, como metais pesados, tem sido largamente usada como um biomarcador na avaliação de risco e biomonitoramento. No presente trabalho foi comparada a extração da fosfatase ácida de P. subcapitata por diferentes métodos e estudada a sua estabilidade, especificidade por substratos, cinética e efeito do Hg 2+ no extrato bruto. O congelamento e descongelamento, associado com ultrassom, foi o método que proporcionou maior rendimento de extração. A enzima, praticamente estável por armazenamento a -20ºC, durante aproximadamente seis meses, demonstrou uma atividade ótima em pH 5 e um valor de Km para o p-nitrofenilfostato (pNPP) de 0,27 mM. Alguns substratos naturais foram hidrolisados com uma intensidade semelhante à do substrato sintético pNPP. Diferentemente dos estudos de exposição a curto prazo (24 horas), observou-se inibição da atividade específica nas culturas expostas durante 7 dias, com um valor de CE 50 (concentração de Hg 2+ que promove 50% de decréscimo da atividade específica) equivalente a 12,63 μM Hg 2+ .

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Section: Cleavage Of Substrates and Phosphatase Inhibitionsupporting

confidence: 69%

Section: Kinetics Studiessupporting

confidence: 69%

Section: Discussion Extractionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Extraction, partial characterization and susceptibility to Hg2+ of acid phosphatase from the microalgae Pseudokirchneriella subcapitata

Jonsson¹,

Aoyama

2009

Sci. agric. (Piracicaba, Braz.)

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“…Acid phosphatases (EC 3.1.3.2), enzymes that catalyze the hydrolysis of a wide range of orthophosphate monoesters, are largely distributed in nature and have been studied in numerous organisms and tissues (Granjeiro et al, 1997;Ferreira et al, 1998aFerreira et al, , 1998bGranjeiro et al, 1999;Fernandes et al, 2003;Jonsson et al, 2007). The enzyme found in mammalian tissues occurs in multiple forms that differ in regard to molecular mass, substrate specificity and sensitivity to inhibitors (Granjeiro et al, 1997).…”

Section: Acid Phosphatase 341 Signaling Featuresmentioning

confidence: 99%

Prostate Cancer Dephosphorylation Atlas

Ferreira¹,

Milani²,

Zambuzzi³

et al. 2011

Prostate Cancer - From Bench to Bedside

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The present textbook highlights many of the exciting discoveries made in the diagnosis and treatment of prostate cancer over the past decade. International thought leaders have contributed to this effort providing a comprehensive and state-of-the art review of the signaling pathways and genetic alterations essential in prostate cancer. This work provides an essential resource for healthcare professionals and scientists dedicated to this field. This textbook is dedicated to the efforts and advances made by our scientific community, realizing we have much to learn in striving to some day in the not too distant future cure this disease particularly among those with an aggressive tumor biology.

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Effect of copper on the activation of the acid phosphatase from the green algae Pseudokirchneriella subcapitata

Jonsson

Aoyama

2009

Biometals

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The presence of copper in water environment may have detrimental effects on aquatic organisms, including algae, where different enzymatic systems can be affected. Algae acid phosphatase plays important roles in metabolic processes such as decomposition of organic phosphate, autophagic digestive process, recycling cellular materials and zygote formation during reproduction. This work describes an in vitro activation effect of copper on the acid phosphatase of the green algae Pseudokirchneriella subcapitata (formely Selenastrum capricornutum) under preincubation condition. Apparent Michaelis constant values of 1.21 and 0.37 mM, and activation energy values of 26.8 and 13.6 kJ mol(-1) were determined in the absence and in the presence of 0.2 mM Cu(2+), respectively. The dissociation constant value for Cu(2+) binding to the enzyme was determined to be 22.04 microM. The decrease of the apparent Michaelis constant (Km) and activation energy values in the presence of Cu(2+) correlates well with its activating effect on the acid phosphatase activity. This propriety could be used as a sensitive bioindicator for copper in environmental samples.

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Bovine kidney low molecular weight acid phosphatase: FMN‐dependent kinetics

Cited by 23 publications

References 9 publications

Extraction, partial characterization and susceptibility to Hg2+ of acid phosphatase from the microalgae Pseudokirchneriella subcapitata

Extraction, partial characterization and susceptibility to Hg2+ of acid phosphatase from the microalgae Pseudokirchneriella subcapitata

Prostate Cancer Dephosphorylation Atlas

Effect of copper on the activation of the acid phosphatase from the green algae Pseudokirchneriella subcapitata

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